Immobilized proteins in buffer imaged at molecular resolution by atomic force microscopy.
Samples of supported planar lipid-protein membranes and actin filaments on mica were imaged by atomic force microscopy (AFM). The samples were fully submerged in buffer at room temperature during imaging. Individual proteins bound to the reconstituted membrane were distinguishable; some structural details could be resolved. Also, surface-induced, self-assembling of actin filaments on mica could be observed. Monomeric subunits were imaged on individual actin filaments. The filaments could be manipulated on or removed from the surface by the tip of the AFM. The process of the decoupling of the filamentous network from the surface upon changing the ionic conditions was imaged in real time.
Weisenhorn
A L
AL
Department of Physics, University of California, Santa Barbara 93106.
Drake
B
B
Prater
C B
CB
Gould
S A
SA
Hansma
P K
PK
Ohnesorge
F
F
Egger
M
M
Heyn
S P
SP
Gaub
H E
HE
D000199:Actins / Q000737:chemistry / Q000648:ultrastructure; D055592:Biophysical Phenomena; D001703:Biophysics; D002021:Buffers; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry / Q000648:ultrastructure; D008853:Microscopy / Q000379:methods; D015394:Molecular Structure; D011506:Proteins / Q000737:chemistry / Q000648:ultrastructure*; D013499:Surface Properties
D000199:Actins; D002021:Buffers; D007140:Immunoglobulin Fab Fragments; D008565:Membrane Proteins; D011506:Proteins